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Effect of the S-to-S bridge on the redox properties and H-2 activation performance of diiron complexes related to the [FeFe]-hydrogenase active site
KTH, Skolan för kemivetenskap (CHE), Kemi, Organisk kemi. KTH, Skolan för kemivetenskap (CHE), Centra, Molekylär elektronik, CMD.ORCID-id: 0000-0002-4521-2870
2016 (engelsk)Inngår i: Dalton Transactions, ISSN 1477-9226, E-ISSN 1477-9234, Vol. 45, nr 44, s. 17687-17696Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Three biomimetic models of the [FeFe]-hydrogenase active site, namely diiron dithiolates of [(mu-edt){Fe(CO)(3)}{Fe(CO)(kappa(2)-PNP)}] (1, edt = ethane-1,2-dithiolate, PNP = Ph2PCH2N(nPr)CH2PPh2), [(mu bdtMe){Fe(CO)(3)}{Fe(CO)(kappa(2)-PNP)}] (2, bdtMe = 4-methylbenzene-1,2-dithiolate), and [(mu-adtBn){Fe(CO)(3)} {Fe(CO)(kappa(2)-PNP)}] (3, adtBn = N-benzyl-2-azapropane-1,3-dithiolate), were prepared and structurally characterized. These complexes feature the same PNP ligand but different S-to-S bridges. Influence of the S-to-S bridge on the electrochemical properties and chemical oxidation reactivity of 1-3 was studied by cyclic voltammetry and by in situ IR spectroscopy. The results reveal that the S-to-S bridge has a considerable effect on the oxidation reactivity of 1-3 and on the stability of in situ generated single-electron oxidized complexes, [1](+), [2](+), and [3](+). The performances of [1](+) and [2](+) for H-2 activation were explored in the presence of a mild chemical oxidant, while rapid decomposition of [3](+) thwarted the further study of this complex. Gratifyingly, 1 was found to be catalytically active, although in a low turnover number, for H-2 oxidation in the presence of excess mild oxidant and a proton trapper under 1 atm H-2 at room temperature.

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ROYAL SOC CHEMISTRY , 2016. Vol. 45, nr 44, s. 17687-17696
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-198599DOI: 10.1039/c6dt02953aISI: 000388104900017PubMedID: 27754505OAI: oai:DiVA.org:kth-198599DiVA, id: diva2:1057587
Forskningsfinansiär
Swedish Energy AgencySwedish Research CouncilKnut and Alice Wallenberg Foundation
Merknad

QC 20161219

Tilgjengelig fra: 2016-12-19 Laget: 2016-12-19 Sist oppdatert: 2017-11-29bibliografisk kontrollert

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